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A novel domain and the new signaling pathway of DgcP in Pseudomonas aeruginosa

Grant number: 24/03134-2
Support Opportunities:Scholarships in Brazil - Doctorate (Direct)
Effective date (Start): March 01, 2024
Effective date (End): March 31, 2028
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal Investigator:Regina Lúcia Baldini
Grantee:Nathan Rodrigues da Silva
Host Institution: Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Associated research grant:21/10577-0 - Biology of Bacteria and Bacteriophages Research Center, AP.CEPID

Abstract

Pseudomonas aeruginosa is an opportunistic pathogen characterized by its ubiquity and antibiotic resistance, as well as being one of the main organisms responsible for nosocomial infections. The transition between planktonic to sessile lifestyles and the biofilm production are mediated by the second messenger c-di-GMP. In previous studies, our group has shown that the Pseudomonas aeruginosa diguanylate cyclase DgcP, an enzyme responsible for c-di-GMP synthesis, interacts with FimV, a scaffold for the type IV pilus machinery (T4P). DgcP presents a conserved, uncharacterized domain in the N-terminal that may regulate its enzymatic activity and interaction with other proteins. The genetic neighborhood of dgcP is conserved in Pseudomonas, suggesting their products may function in an unidentified signaling pathway. Among these genes are dsbA (a periplasmic thioredoxin), a phosphodiesterase with a CSS motif (sensor domain regulated by disulfide bonds in periplasm), cytochrome c4 (a periplasmic electron carrier), a putative enzyme of the exo/endonuclease phosphatase superfamily and a predicted peptidoglycan binding amidase. We observed that a dgcP mutant is more sensitive to oxidative stress than the wild type, suggesting a role of dgcP in the response. These genes are also involved in biofilm production under sub inhibitory concentrations of antibiotics and the porin OprF is a target of DsbA. Therefore, we hypothesize an intersection between c-di-GMP signaling, oxidative stress and the OprF/SigX system. (AU)

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